Evidence map›Paper›PMID 9882677›Full record

ArticleJournal of bacteriology1999

A polypeptide with similarity to phycocyanin alpha-subunit phycocyanobilin lyase involved in degradation of phycobilisomes.

N Dolganov, A R Grossman

Open access · bronzeAbstract read
In one paragraph

Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 90 citations in OpenAlex.

  1. Article
  2. Article
  3. Discovery of a small protein factor involved in the coordinated degradation of phycobilisomes in cyanobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  4. Review
  5. Article
  6. Complete Genome Sequence and Comparative Analysis ofInternational journal of molecular sciences · 2019
    Article
  7. Structures and enzymatic mechanisms of phycobiliprotein lyases CpcE/F and PecE/F.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Interactions of Freshwater Cyanobacteria with Bacterial Antagonists.Applied and environmental microbiology · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Phycobilin:cystein-84 biliprotein lyase, a near-universal lyase for cysteine-84-binding sites in cyanobacterial phycobiliproteins.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Article
  19. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

N DolganovDepartment of Plant Biology, The Carnegie Institution of Washington, Stanford, California 94305, USA.
A R Grossman
Carnegie Institution for Science · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To optimize the utilization of photosynthate and avoid damage that can result from the absorption of excess excitation energy, photosynthetic organisms must rapidly modify the synthesis and activities of components of the photosynthetic apparatus in response to environmental cues. During nutrient-limited growth, cyanobacteria degrade their light-harvesting complex, the phycobilisome, and dramatically reduce the rate of photosynthetic electron transport. In this report, we describe the isolation and characterization of a cyanobacterial mutant that does not degrade its phycobilisomes during either sulfur or nitrogen limitation and exhibits an increased ratio of phycocyanin to chlorophyll during nutrient-replete growth. The mutant phenotype was complemented by a gene encoding a polypeptide with similarities to polypeptides that catalyze covalent bond formation between linear tetrapyrrole chromophores and subunits of apophycobiliproteins. The complementing gene, designated nblB, is expressed at approximately the same level in cells grown in nutrient-replete medium and medium devoid of either sulfur or nitrogen. These results suggest that the NblB polypeptide may be a constitutive part of the machinery that coordinates phycobilisome degradation with environmental conditions.

Indexed as

Amino Acid SequenceBacterial ProteinsCyanobacteriaGenetic Complementation TestGenome, BacterialLight-Harvesting Protein ComplexesLyasesMolecular Sequence DataMutagenesisOpen Reading FramesPhenotypePhycobilisomesPlant ProteinsPlasmidsSequence AlignmentSequence Homology, Amino AcidBacterial ProteinsLight-Harvesting Protein ComplexesLyasesNblB protein, Synechococcus sp.Phycobilisomesphycocyanin alpha-subunit phycocyanobilin lyasePlant Proteins

Identifiers

PMID9882677
PMCPMC93417
OpenAlexW2125860910

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.